ID   CAPP_MARMS              Reviewed;         876 AA.
AC   A6VUQ5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Mmwyl1_1255;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP000749; ABR70184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VUQ5; -.
DR   SMR; A6VUQ5; -.
DR   STRING; 400668.Mmwyl1_1255; -.
DR   KEGG; mmw:Mmwyl1_1255; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..876
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000082429"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   876 AA;  98839 MW;  A29755A1669E9AE1 CRC64;
     MSDSQASLRE NVRLLGDCLG ESMSNHLGEG FLEKVENIRL LSKNGRQSGD SAALIQALEA
     LDDKEIVPVA RAFNQFLNLS NIAEQYHRVH RRRTNESLGV YHNPVGDLLT RLSKQSFTAE
     QMISSLQSQS IELVLTAHPT EVVRRSLIRK YDNISSELEA LDKDNILPLE ETKHIRRLKE
     IITQAWHTDE IREDRPTPVD EAKWGFAVIE QSLWQAVPRF FRQLDEQFSE FSKEDRLPLD
     LAPIRFATWM GGDRDGNPNV THKVTKEVTL LARWMAADLY IKDLNVLRSE FSMTQCNEAL
     RARVGDSAQP YREVLRHLEN KMLATKNWAK ACLDGKPTSG EDIFLDIQEL TDDLILCYQS
     LLDCGMKVIA NGSLLDLIRC AATFGATLVR LDVRQDASRH IDALSAITRF YGLGDYAEWD
     EASRQAFLLT ELNSKRPLLP MEWTPTAEVK EVLDTFAMIS QGQQNSFGSY VISMASAPSD
     VLAVALMLKE SGVGFPMRIV PLFETLADLD NAEPIIEQLF SIPWYKSYIN GRQEVMIGYS
     DSAKDAGQIA ATWGQYRAQE ALTRLCKKHG IHLTLFHGRG GTVGRGGGPA HVAILSQPPG
     SVNGAIRVTE QGEMIRFKFG IPDIAVRSLE LYCSAVMEAS LIPAEPPKEE WRAIMDEMAE
     VGMNQYRSII RGHEDFVPYF RATTPEQELA KLPLGSRPAR RRSDGGVESL RAIPWIFAWM
     QIRLMLPAWL GAESALQQGV ESGNLEKLRE MHKKWPFFGA YLDMLDMVLA KAEPEIAEYY
     EKRLVGEELQ GLGRLLRGKL KQVSELVKML KKQERLIEDN KTIRQSIDVR NPYIDPLHYL
     QAELLYRSRK DEENAEVNKA LMITMAGIAS GMQNTG
//